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1h4p
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(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4p RCSB], [http://www.ebi.ac.uk/pdbsum/1h4p PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4p RCSB], [http://www.ebi.ac.uk/pdbsum/1h4p PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EXG1_YEAST EXG1_YEAST]] Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:09, 25 December 2014
CRYSTAL STRUCTURE OF EXO-1,3-BETA GLUCANSE FROM SACCHAROMYCES CEREVISIAE
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